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Volumn 71, Issue 3, 2006, Pages

Frozen stability of fish protein isolate under various storage conditions

Author keywords

Alkali treated protein isolates; Cryoprotectant; DSC; Frozen storage; Surface hydrophobicity

Indexed keywords


EID: 33646377204     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2006.tb15622.x     Document Type: Article
Times cited : (43)

References (45)
  • 2
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescence probes
    • Alizadeh-Pasdar N, Li-Chan ECY. 2000. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescence probes. J Agric Food Chem 48:328-34.
    • (2000) J Agric Food Chem , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 3
    • 0011807556 scopus 로고
    • Denaturation of cod myosin during freezing after modification with formaldehyde
    • Ang JF, Hultin HO. 1989. Denaturation of cod myosin during freezing after modification with formaldehyde. J Food Sci 54:814-8.
    • (1989) J Food Sci , vol.54 , pp. 814-818
    • Ang, J.F.1    Hultin, H.O.2
  • 4
    • 0020477047 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T, Timasheff SN. 1982. Stabilization of protein structure by sugars. Biochemistry 21:6545-52.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 5
    • 0036150757 scopus 로고    scopus 로고
    • A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage
    • Badii F, Howell NK. 2002. A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage. J Sci Food Agric 82(1):87-97.
    • (2002) J Sci Food Agric , vol.82 , Issue.1 , pp. 87-97
    • Badii, F.1    Howell, N.K.2
  • 6
    • 0037467080 scopus 로고    scopus 로고
    • Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry
    • Badii F, Howell NK. 2003. Elucidation of the effect of formaldehyde and lipids on frozen stored cod collagen by FT-Raman spectroscopy and differential scanning calorimetry. J Agric Food Chem 51:1440-6.
    • (2003) J Agric Food Chem , vol.51 , pp. 1440-1446
    • Badii, F.1    Howell, N.K.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 84986430573 scopus 로고
    • Accelerated denaturation of myosin in frozen solution
    • Buttkus H. 1970. Accelerated denaturation of myosin in frozen solution. J Food Sci 35:558-62.
    • (1970) J Food Sci , vol.35 , pp. 558-562
    • Buttkus, H.1
  • 9
    • 0031433220 scopus 로고    scopus 로고
    • Structural changes in cod myosin after modification with formaldehyde or frozen storage
    • Careche M, Li-Chan ECY. 1997. Structural changes in cod myosin after modification with formaldehyde or frozen storage. J Food Sci 62:717-23.
    • (1997) J Food Sci , vol.62 , pp. 717-723
    • Careche, M.1    Li-Chan, E.C.Y.2
  • 10
    • 0036812288 scopus 로고    scopus 로고
    • Acid-aided protein recovery from enzyme-rich pacific whiting
    • Choi YJ, Park JW. 2002. Acid-aided protein recovery from enzyme-rich pacific whiting. J Food Sci 67:2962-7.
    • (2002) J Food Sci , vol.67 , pp. 2962-2967
    • Choi, Y.J.1    Park, J.W.2
  • 12
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins
    • Fennema OR, editor. New York: Marcel Dekker, Inc.
    • Damodaran S. 1996. Amino acids, peptides, and proteins. In: Fennema OR, editor. Food chemistry. 3rd ed. New York: Marcel Dekker, Inc. p 321-429.
    • (1996) Food Chemistry. 3rd Ed. , pp. 321-429
    • Damodaran, S.1
  • 14
    • 0000416821 scopus 로고
    • Role of formaldehyde in formation of natural actomyosin aggregates in Hake during frozen storage
    • Del Mazo ML, Huidobro A, Torrejon P, Tejada M, Careche M. 1994. Role of formaldehyde in formation of natural actomyosin aggregates in Hake during frozen storage. Z Lebensm Unters Forsch 198:459-64.
    • (1994) Z Lebensm Unters Forsch , vol.198 , pp. 459-464
    • Del Mazo, M.L.1    Huidobro, A.2    Torrejon, P.3    Tejada, M.4    Careche, M.5
  • 16
    • 0002423563 scopus 로고
    • Biochemical reactions in fish muscle during frozen storage
    • Bligh EG, editor. Cornwall, U.K.: Fishing News Books
    • Haard NF. 1992. Biochemical reactions in fish muscle during frozen storage. In: Bligh EG, editor. Seafood science and technology. Cornwall, U.K.: Fishing News Books, p 176-209.
    • (1992) Seafood Science and Technology , pp. 176-209
    • Haard, N.F.1
  • 17
    • 3042652596 scopus 로고
    • Variation of SH content and kamaboko-gel forming ability of shark muscle protein by electrolysis
    • Hamada M, Ishizaki S, Nagai T. 1994. Variation of SH content and kamaboko-gel forming ability of shark muscle protein by electrolysis. J Shimonoseki Univ Fish 42:131-5.
    • (1994) J Shimonoseki Univ Fish , vol.42 , pp. 131-135
    • Hamada, M.1    Ishizaki, S.2    Nagai, T.3
  • 18
    • 84985273101 scopus 로고
    • Differential scanning calorimetry of fish muscle: The effect of processing and species variation
    • Hastings RI, Rodger GW, Park R, Matthews AD, Anderson EM. 1985. Differential scanning calorimetry of fish muscle: The effect of processing and species variation. J Food Sci 50:503-6, 510.
    • (1985) J Food Sci , vol.50 , pp. 503-506
    • Hastings, R.I.1    Rodger, G.W.2    Park, R.3    Matthews, A.D.4    Anderson, E.M.5
  • 19
    • 84988113025 scopus 로고
    • Thermal stability of fish myofibrils: A differential scanning calorimetric study
    • Howell BK, Matthews AD, Donnelly AP. 1991. Thermal stability of fish myofibrils: a differential scanning calorimetric study. Int J Food Sci Technol 26:283-95.
    • (1991) Int J Food Sci Technol , vol.26 , pp. 283-295
    • Howell, B.K.1    Matthews, A.D.2    Donnelly, A.P.3
  • 21
    • 0347694884 scopus 로고    scopus 로고
    • New approaches for the effective recovery of fish proteins and their physicochemical characteristics
    • Kim YS, Park JW, Choi YJ. 2003. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fisheries Sci 69:1231-9.
    • (2003) Fisheries Sci , vol.69 , pp. 1231-1239
    • Kim, Y.S.1    Park, J.W.2    Choi, Y.J.3
  • 22
    • 0242607667 scopus 로고    scopus 로고
    • Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding
    • Kristinsson HG, Hultin HO. 2003a. Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J Agric Food Chem 51:7187-96.
    • (2003) J Agric Food Chem , vol.51 , pp. 7187-7196
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 23
    • 0037392919 scopus 로고    scopus 로고
    • Effect of low and high pH treatment on the functional properties of cod muscle proteins
    • 917tu:-22
    • Kristinsson HG, Hultin HO. 2003b. Effect of low and high pH treatment on the functional properties of cod muscle proteins. J Food Sci 68:917tu:-22.
    • (2003) J Food Sci , vol.68
    • Kristinsson, H.G.1    Hultin, H.O.2
  • 24
    • 84985200262 scopus 로고
    • Separation of cod (Gadus morhua) fillet proteins by electrophoresis and HPLC after various frozen storage treatments
    • LeBlanc EL, LeBlanc RI. 1989. Separation of cod (Gadus morhua) fillet proteins by electrophoresis and HPLC after various frozen storage treatments. J Food Sci 54:827-34.
    • (1989) J Food Sci , vol.54 , pp. 827-834
    • LeBlanc, E.L.1    LeBlanc, R.I.2
  • 25
    • 0026592952 scopus 로고
    • Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage
    • LeBlanc EL, LeBlanc RJ. 1992. Determination of hydrophobicity and reactive groups in proteins of cod (Gadus morhua) muscle during frozen storage. Food Chem 43:3-11.
    • (1992) Food Chem , vol.43 , pp. 3-11
    • LeBlanc, E.L.1    LeBlanc, R.J.2
  • 26
    • 0002834962 scopus 로고
    • Surimi process technology
    • Lee CM. 1984. Surimi process technology. Food Technol 38(11):69-80.
    • (1984) Food Technol , vol.38 , Issue.11 , pp. 69-80
    • Lee, C.M.1
  • 27
    • 84986517574 scopus 로고
    • Protein insolubilization in frozen Greenland halibut (Reinhardtius hippoglossoides)
    • Lim HK, Haard NF. 1984. Protein insolubilization in frozen Greenland halibut (Reinhardtius hippoglossoides). J Food Biochem 8:163-87.
    • (1984) J Food Biochem , vol.8 , pp. 163-187
    • Lim, H.K.1    Haard, N.F.2
  • 28
    • 0000812301 scopus 로고
    • Carbohydrates as cryoprotectants for meats and surimi
    • MacDonald GA, Lanier TC. 1991. Carbohydrates as cryoprotectants for meats and surimi. Food Technol 45(3):151-9.
    • (1991) Food Technol , vol.45 , Issue.3 , pp. 151-159
    • MacDonald, G.A.1    Lanier, T.C.2
  • 29
    • 84948501135 scopus 로고
    • The effects of freezing on fish proteins
    • Mackie IM. 1993. The effects of freezing on fish proteins. Food Rev Int 9:575-610.
    • (1993) Food Rev Int , vol.9 , pp. 575-610
    • Mackie, I.M.1
  • 30
    • 0002120573 scopus 로고
    • Chemical deterioration of muscle proteins during frozen storage
    • Whitaker JR, Fujimoto M, editors. ACS Symposium Series 123. Washington, D.C.: American Chemical Society
    • Matsumoto JJ. 1980. Chemical deterioration of muscle proteins during frozen storage. In: Whitaker JR, Fujimoto M, editors. Chemical deterioration of proteins. ACS Symposium Series 123. Washington, D.C.: American Chemical Society.
    • (1980) Chemical Deterioration of Proteins
    • Matsumoto, J.J.1
  • 31
    • 0001021712 scopus 로고
    • Cryostabilization of protein in surimi
    • Lanier TC, Lee CM, editors. New York: Marcel Dekker Inc.
    • Matsumoto JJ, Noguchi SF. 1992, Cryostabilization of protein in surimi. In: Lanier TC, Lee CM, editors. Surimi technology. New York: Marcel Dekker Inc. p 357-88.
    • (1992) Surimi Technology , pp. 357-388
    • Matsumoto, J.J.1    Noguchi, S.F.2
  • 32
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan FJ, German JB, Kinsella, JE. 1995. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. J Agric Food Chem 43:46-52.
    • (1995) J Agric Food Chem , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 33
    • 85008080177 scopus 로고
    • Exposure of hydrophobic amino acid residues from actomyosin on freezing. Reconfirmation by fluorometry
    • Niwa E, Kohda S, Kanoh S, Nakayama T. 1986. Exposure of hydrophobic amino acid residues from actomyosin on freezing. Reconfirmation by fluorometry. Bull Jpn Soc Sci Fish 52:1039-42.
    • (1986) Bull Jpn Soc Sci Fish , vol.52 , pp. 1039-1042
    • Niwa, E.1    Kohda, S.2    Kanoh, S.3    Nakayama, T.4
  • 35
    • 84987299744 scopus 로고
    • Cryoprotective effects of sugar, polyols and/or phosphate on Alaska pollock surimi
    • Park JW, Lanier TC, Green DP. 1988. Cryoprotective effects of sugar, polyols and/or phosphate on Alaska pollock surimi. J Food Sci 53:1-3.
    • (1988) J Food Sci , vol.53 , pp. 1-3
    • Park, J.W.1    Lanier, T.C.2    Green, D.P.3
  • 36
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid) - A reexamination
    • Riddles PW, Blakeley RL, Zerner B. 1979. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)-a reexamination. Anal Biochem 94:75-81.
    • (1979) Anal Biochem , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 37
    • 0034775207 scopus 로고    scopus 로고
    • Structural changes in actomyosin and surimi from ling cod (Ophiodon elongates) during frozen storage in the absence and presence of cryoprotectants
    • Sultanbawa Y, Li-Chan ECY. 2001. Structural changes in actomyosin and surimi from ling cod (Ophiodon elongates) during frozen storage in the absence and presence of cryoprotectants. J Agric Food Chem 49:4716-25.
    • (2001) J Agric Food Chem , vol.49 , pp. 4716-4725
    • Sultanbawa, Y.1    Li-Chan, E.C.Y.2
  • 38
    • 84987358424 scopus 로고
    • Cryoprotective effects of lactitol, paltinit, and polydextrose on cod surimi proteins during frozen storage
    • Sych J, Lacroix C, Adambounou LT, Castaigne F. 1990. Cryoprotective effects of lactitol, paltinit, and polydextrose on cod surimi proteins during frozen storage. J Food Sci 55:356-60.
    • (1990) J Food Sci , vol.55 , pp. 356-360
    • Sych, J.1    Lacroix, C.2    Adambounou, L.T.3    Castaigne, F.4
  • 39
    • 33646380702 scopus 로고
    • Relation between the quality of frozen surimi (fish paste) from Alaska pollack and various sugar content
    • Takayoshi K. 1977. Relation between the quality of frozen surimi (fish paste) from Alaska pollack and various sugar content. Hokusuishi Geppo 34(5):11-6.
    • (1977) Hokusuishi Geppo , vol.34 , Issue.5 , pp. 11-16
    • Takayoshi, K.1
  • 42
    • 3042579438 scopus 로고    scopus 로고
    • Role of pH in solubility and conformational changes of Pacific whiting muscle proteins
    • Thawornchinsombut S, Park JW. 2004. Role of pH in solubility and conformational changes of Pacific whiting muscle proteins. J Food Biochem 28:135-54.
    • (2004) J Food Biochem , vol.28 , pp. 135-154
    • Thawornchinsombut, S.1    Park, J.W.2
  • 43
    • 0021396951 scopus 로고
    • Differential scanning calorimetric study of muscle and its proteins: Myosin and its subfragments [rabbit]
    • Wright DJ, Wilding P. 1984. Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments [rabbit]. J Sci Food Agric 35:357-72.
    • (1984) J Sci Food Agric , vol.35 , pp. 357-372
    • Wright, D.J.1    Wilding, P.2
  • 44
    • 4744341461 scopus 로고    scopus 로고
    • Effects of alkaline and acid solubilization on gelation characteristics of Rockfish muscle proteins
    • Yongsawatdigul J, Park JW. 2004. Effects of alkaline and acid solubilization on gelation characteristics of Rockfish muscle proteins. J Food Sci 69:449-505.
    • (2004) J Food Sci , vol.69 , pp. 449-505
    • Yongsawatdigul, J.1    Park, J.W.2
  • 45
    • 84987357859 scopus 로고
    • Cryoprotectant effects in surimi and surimi/mince-based extruded products
    • Yoon KS, Lee CM. 1990. Cryoprotectant effects in surimi and surimi/mince-based extruded products. J Food Sci 55:1210-6.
    • (1990) J Food Sci , vol.55 , pp. 1210-1216
    • Yoon, K.S.1    Lee, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.